Abstract
Prolyl hydroxylase is an enzyme which oxidatively modifies the proline residue of hypoxia inducible factor (HIF-lα) in the presence of oxygen in an apparently irreversible reaction. This reaction also requires labile Fe2+, 2-oxogluterate (2-OG) and ascorbic acid. Hypoxia retards this reaction and HIF-1α is accumulated. Similarly, Fe2+ chelation mimics hypoxia-like effect. Thus, the enzyme stands at the gateway between hypoxia and normoxia. The hy-droxylated HIF-1α undergoes proteasomal degradation during normoxia whereas HIF-1α, accumulated during hypoxia, binds with β-subunits to form HIF-1 which is then transcripted to various genes in the nucleus.
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© 2004 Kluwer Academic/Plenum Publishers, New York
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Lahiri, S., Roy, A., Li, J., Baby, S.M., Mokashi, A., Di Giulio, C. (2004). Role of Fe2+ in Oxygen Sensing in the Carotid Body. In: Champagnat, J., Denavit-Saubié, M., Fortin, G., Foutz, A.S., Thoby-Brisson, M. (eds) Post-Genomic Perspectives in Modeling and Control of Breathing. Advances in Experimental Medicine and Biology, vol 551. Springer, Boston, MA. https://doi.org/10.1007/0-387-27023-X_10
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DOI: https://doi.org/10.1007/0-387-27023-X_10
Publisher Name: Springer, Boston, MA
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